Detoxification of isothiocyanate allelochemicals by glutathione transferase in three lepidopterous species.

Glutathione transferase activity towards various plant isothiocyanates was studied in larvae of the two generalists, fall armyworm [Spodoptera frugiperda (J.E. Smith)], and cabbage looper [Trichoplusia ni (Hübner)], and the specialist, velvetbean caterpillar (Anticarsia gemmatalis Hübner) using the midgut soluble fraction as enzyme source. The generalists, but not the specialist, are adapted to feeding on isothiocyanate-containing crucifers. Allyl and benzyl isothiocyanate were found to be metabolized by glutathione transferase from the two generalist species, but no activity was detected with the specialist. The transferase activity towards these allelochemicals in the cabbage looper was two- to sixfold higher than that in the fall armyworm. In all instances, activity was induced by various allelochemicals including indole 3-acetonitrile, indole 3-carbinol, flavone, xanthotoxin, and its own substrates. The induction ranged from 1.3- to 10.1-fold depending on the allelochemical, with the fall armyworm being more inducible. The transferase system of fall armyworm also metabolized another analog, 2-phenylethyl isothiocyanate, but activity can only be observed after induction. Bioassay results showed that these isothiocyanates were all toxic to the lepidopterans, causing acute toxicity in neonates and final-instar larvae. The results suggest that glutathione transferase plays an important role in the detoxification of isothiocyanates and hence food-plant adaptation in phytophagous insects.